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A sliding clamp monkey wrench

Crystal structures of the Escherichia coli DNA replication γ clamp loading complex and of a subunit of the clamp loader bound to a β clamp monomer provide a physical framework in which to view ATP-dependent modulation of γ complex–β interactions. The structural data suggest how the β ring is opened and loaded onto DNA in the absence of a direct interaction between the γ complex and the β dimer interface.

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Figure 1: Schematic diagram of the E. coli replisome containing a dimeric polymerase capable of coordinated leading and lagging strand synthesis.
Figure 2: Ribbon diagrams based on crystal structures of sliding clamps from a, E. coli (β)3, b, humans (PCNA)5, and c, bacteriophage T4 (gp45)6.
Figure 3: Schematic diagram of the δ–β interaction that results in clamp opening.
Figure 4: Schematic diagram of the ATP-induced conformational change in the E. coli clamp loader2.

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Correspondence to Linda B. Bloom.

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Bloom, L., Goodman, M. A sliding clamp monkey wrench. Nat Struct Mol Biol 8, 829–831 (2001). https://doi.org/10.1038/nsb1001-829

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